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2PL9

Crystal Structure of CheY-Mg(2+)-BeF(3)(-) in Complex with CheZ(C19) Peptide solved from a P2(1)2(1)2 Crystal

Functional Information from GO Data
ChainGOidnamespacecontents
A0000155molecular_functionphosphorelay sensor kinase activity
A0000160biological_processphosphorelay signal transduction system
A0005737cellular_componentcytoplasm
A0006935biological_processchemotaxis
A0009927molecular_functionhistidine phosphotransfer kinase activity
A0046872molecular_functionmetal ion binding
A0097588biological_processarchaeal or bacterial-type flagellum-dependent cell motility
B0000155molecular_functionphosphorelay sensor kinase activity
B0000160biological_processphosphorelay signal transduction system
B0005737cellular_componentcytoplasm
B0006935biological_processchemotaxis
B0009927molecular_functionhistidine phosphotransfer kinase activity
B0046872molecular_functionmetal ion binding
B0097588biological_processarchaeal or bacterial-type flagellum-dependent cell motility
C0000155molecular_functionphosphorelay sensor kinase activity
C0000160biological_processphosphorelay signal transduction system
C0005737cellular_componentcytoplasm
C0006935biological_processchemotaxis
C0009927molecular_functionhistidine phosphotransfer kinase activity
C0046872molecular_functionmetal ion binding
C0097588biological_processarchaeal or bacterial-type flagellum-dependent cell motility
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 130
ChainResidue
AASP13
AASP57
AASN59
ABEF131
AHOH132
AHOH144

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 130
ChainResidue
BBEF131
BHOH133
BHOH134
BASP13
BASP57
BASN59

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 130
ChainResidue
CASP13
CASP57
CASN59
CBEF131
CHOH132
CHOH133

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BEF A 131
ChainResidue
AASP57
ATRP58
AASN59
ATHR87
AALA88
ALYS109
AMG130

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BEF B 131
ChainResidue
BASP57
BTRP58
BASN59
BTHR87
BALA88
BLYS109
BMG130
BHOH133

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MES B 132
ChainResidue
BASP3
CASP13
CPHE14
CSER15

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BEF C 131
ChainResidue
CASP57
CTRP58
CASN59
CTHR87
CALA88
CLYS109
CMG130
CHOH132

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A0A0H3AMJ9
ChainResidueDetails
AASP12
BASP12
CASP12

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:16674976, ECO:0000269|PubMed:18083806, ECO:0000269|PubMed:8257674, ECO:0007744|PDB:2CHE, ECO:0007744|PDB:2FKA, ECO:0007744|PDB:2FLW, ECO:0007744|PDB:2FMH, ECO:0007744|PDB:2FMK, ECO:0007744|PDB:2PL9, ECO:0007744|PDB:2PMC
ChainResidueDetails
AASP13
AASP57
AASN59
BASP13
BASP57
BASN59
CASP13
CASP57
CASN59

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:1902474, ECO:0000269|PubMed:3280143
ChainResidueDetails
AASP57
BASP57
CASP57

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000250
ChainResidueDetails
ALYS92
ALYS109
BLYS92
BLYS109
CLYS92
CLYS109

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PDB entries from 2024-04-24

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